ID RNPH_BRUSI Reviewed; 238 AA. AC B0CJ32; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 1. DT 16-JUN-2009, entry version 11. DE RecName: Full=Ribonuclease PH; DE Short=RNase PH; DE EC=2.7.7.56; DE AltName: Full=tRNA nucleotidyltransferase; GN Name=rph; OrderedLocusNames=BSUIS_A0174; OS Brucella suis (strain ATCC 23445 / NCTC 10510). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=470137; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., RA Dharmanolla C., Gillespie J.J., Kenyon R.W., Lu J., Mane S., RA Mohapatra S., Nagrani S., Purkayastha A., Rajasimha H.K., RA Shallom J.M., Shallom S., Shukla M., Snyder E.E., Sobral B.W., RA Wattam A.R., Will R., Williams K., Yoo H., Bruce D., Detter C., RA Munk C., Brettin T.S.; RT "Brucella suis ATCC 23445 whole genome shotgun sequencing project."; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Phosphorolytic exoribonuclease that removes nucleotide CC residues following the -CCA terminus of tRNA and adds nucleotides CC to the ends of RNA molecules by using nucleoside diphosphates as CC substrates (By similarity). CC -!- CATALYTIC ACTIVITY: tRNA(n+1) + phosphate = tRNA(n) + a nucleoside CC diphosphate. CC -!- SIMILARITY: Belongs to the RNase PH family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000911; ABY37276.1; -; Genomic_DNA. DR RefSeq; YP_001626846.1; -. DR GeneID; 5838331; -. DR GenomeReviews; CP000911_GR; BSUIS_A0174. DR KEGG; bmt:BSUIS_A0174; -. DR OMA; B0CJ32; YAMLPRA. DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:InterPro. DR GO; GO:0000049; F:tRNA binding; IEA:HAMAP. DR GO; GO:0009022; F:tRNA nucleotidyltransferase activity; IEA:HAMAP. DR GO; GO:0004549; F:tRNA-specific ribonuclease activity; IEA:InterPro. DR GO; GO:0008033; P:tRNA processing; IEA:HAMAP. DR HAMAP; MF_00564; -; 1. DR InterPro; IPR001247; ExoRNase_PH_dom1. DR InterPro; IPR015847; ExoRNase_PH_dom2. DR InterPro; IPR018336; Ribonuclease-PH_CS. DR InterPro; IPR002381; RNase_PH_bac-type. DR Pfam; PF01138; RNase_PH; 1. DR Pfam; PF03725; RNase_PH_C; 1. DR TIGRFAMs; TIGR01966; RNasePH; 1. DR PROSITE; PS01277; RIBONUCLEASE_PH; 1. PE 3: Inferred from homology; KW Complete proteome; Nucleotidyltransferase; Transferase; KW tRNA processing. FT CHAIN 1 238 Ribonuclease PH. FT /FTId=PRO_1000082284. SQ SEQUENCE 238 AA; 25907 MW; 70CAF4B8F47A8E9C CRC64; MRPSKRAADE MRAISFERGV SKHAEGSCLV KFGDTHVLCT ASLEEKVPGW MRNTGKGWVT AEYGMLPRST GERMRREAAA GKQGGRTQEI QRLIGRSLRA VVDMQALGEM QITVDCDVIQ ADGGTRTAAI TGGWVALHEC LRWMEARQMV RVEKVLKDHV AAISCGIYEG VPVLDLDYAE DSVAETDSNF VMTGKGGIVE IQGTAEGVPF SEEEFGALMK LARSGIDRLV SLQKMAVA //